Evidence map›Paper›PMID 35579296›Full record

ReviewBioscience reports2022

Regulation and function of elF2B in neurological and metabolic disorders.

Filipe M Hanson, Rachel E Hodgson, Madalena I Ribeiro de Oliveira, K Elizabeth Allen, Susan Gerarda Campbell

Open access · goldAbstract readReview
In one paragraph

Review in Bioscience reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.8field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 34 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Filipe M HansonBiomolecular Sciences Research Centre, Industry and Innovation Research Institute, Sheffield Hallam University, Sheffield, S1 1WB, U.K.
Rachel E HodgsonBiomolecular Sciences Research Centre, Industry and Innovation Research Institute, Sheffield Hallam University, Sheffield, S1 1WB, U.K.
Madalena I Ribeiro de OliveiraBiomolecular Sciences Research Centre, Industry and Innovation Research Institute, Sheffield Hallam University, Sheffield, S1 1WB, U.K.
K Elizabeth AllenBiomolecular Sciences Research Centre, Industry and Innovation Research Institute, Sheffield Hallam University, Sheffield, S1 1WB, U.K.
Susan Gerarda CampbellBiomolecular Sciences Research Centre, Industry and Innovation Research Institute, Sheffield Hallam University, Sheffield, S1 1WB, U.K.ORCID 0000-0002-6740-1445
Sheffield Hallam University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic initiation factor 2B, eIF2B is a guanine nucleotide exchange, factor with a central role in coordinating the initiation of translation. During stress and disease, the activity of eIF2B is inhibited via the phosphorylation of its substrate eIF2 (p-eIF2α). A number of different kinases respond to various stresses leading to the phosphorylation of the alpha subunit of eIF2, and collectively this regulation is known as the integrated stress response, ISR. This targeting of eIF2B allows the cell to regulate protein synthesis and reprogramme gene expression to restore homeostasis. Advances within structural biology have furthered our understanding of how eIF2B interacts with eIF2 in both the productive GEF active form and the non-productive eIF2α phosphorylated form. Here, current knowledge of the role of eIF2B in the ISR is discussed within the context of normal and disease states focusing particularly on diseases such as vanishing white matter disease (VWMD) and permanent neonatal diabetes mellitus (PNDM), which are directly linked to mutations in eIF2B. The role of eIF2B in synaptic plasticity and memory formation is also discussed. In addition, the cellular localisation of eIF2B is reviewed and considered along with the role of additional in vivo eIF2B binding factors and protein modifications that may play a role in modulating eIF2B activity during health and disease.

Indexed as

Eukaryotic Initiation Factor-2BMetabolic DiseasesHumansInfant, NewbornPhosphorylationEukaryotic Initiation Factor-2Bcellular targetingeukaryotic gene expressionProtein synthesisstress responseTranslational Control

Identifiers

PMID35579296
PMCPMC9208314
OpenAlexW4280576604

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.